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Eukaryotic translation initiation factor 2, subunit 3, structural gene X-linked

pp42, eIF2gamma, GCD11
The protein encoded by this gene is the largest subunit of a heterotrimeric GTP-binding protein involved in the recruitment of methionyl-tRNA(i) to the 40 S ribosomal subunit. [provided by RefSeq, Jan 2010] (from NCBI)
Top mentioned proteins: ACID, eIF2B, HAD, Insulin, V1a
Papers on pp42
A small molecule angiotensin II type 2 receptor (AT₂R) antagonist produces analgesia in a rat model of neuropathic pain by inhibition of p38 mitogen-activated protein kinase (MAPK) and p44/p42 MAPK activation in the dorsal root ganglia.
Walther et al., Brisbane, Australia. In Pain Med, 2013
Mean DRG IF levels for activated p38 (pp38) and activated p44/p42 (pp44/pp42) MAPK were also increased ∼1.5-2.0-fold
Effects of angiotensin II type 2 receptor overexpression on the growth of hepatocellular carcinoma cells in vitro and in vivo.
Li et al., Guangzhou, China. In Plos One, 2012
The data also indicate that overexpression of AT2R led to apoptosis via cell death signaling pathway that is dependent on activation of p38 MAPK, pJNK, caspase-8 and caspase-3 and inactivation of pp42/44 MAPK (Erk1/2).
Translation initiation factor 2gamma mutant alters start codon selection independent of Met-tRNA binding.
Dever et al., Bethesda, United States. In Mol Cell Biol, 2008
Data suggest that structural alterations in eIF2gamma subtly alter the conformation of Met-tRNA(i)(Met) on the 40S subunit and thereby affect the fidelity of start codon recognition independent of Met-tRNA(i)(Met) binding affinity.
Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states.
Schmitt et al., Palaiseau, France. In Proc Natl Acad Sci U S A, 2007
Recently, it has been proposed that dissociation of eIF2 from the initiation complex is closely coupled to that of Pi from eIF2gamma upon start codon recognition.
Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2beta and -2gamma mediate guanine nucleotide exchange.
Pavitt et al., Manchester, United Kingdom. In Mol Cell Biol, 2007
One of the most complicated pairs is eukaryotic initiation factor 2B (eIF2B) and eIF2, which function during protein synthesis initiation in eukaryotes.
Site-specific effect of estradiol on gene expression in the adipose tissue of ob/ob mice.
Shimokado et al., Tokyo, Japan. In Horm Metab Res, 2007
DEAD-box Y RNA helicase (DBY) and eukaryotic initiation factor 2 gamma Y (eIF2gamma Y) were expressed only in male adipose tissue.
The N-terminal lysine residue-rich domain II and the 340-430 amino acid segment of eukaryotic initiation factor 2-associated glycoprotein p67 are the binding sites for the gamma-subunit of eIF2.
Datta et al., Kent, United States. In Exp Cell Res, 2006
To understand the molecular details of interaction between p67 and the subunits of eIF2, we applied several biochemical and mutational analyses to identify interacting domains within p67 and eIF2gamma.
The binding between p67 and eukaryotic initiation factor 2 plays important roles in the protection of eIF2alpha from phosphorylation by kinases.
Majumdar et al., Kent, United States. In Arch Biochem Biophys, 2006
KRC-7 cells constitutively expressing the D6/2 mutant showed slightly decreased levels of PKR phosphorylation and significantly low level of phosphorylation of ERKs 1 and 2. The D6/2 mutant also showed increased binding with eIF2alpha and eIF2gamma and almost similar binding with ERKs 1 and 2 as compared to wild type p67.
Direct binding of translation initiation factor eIF2gamma-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B epsilon.
Dever et al., Bethesda, United States. In J Biol Chem, 2006
The GTP-binding (G) domain resides in the gamma subunit of the heterotrimeric eIF2; however, only eIF2beta, and not eIF2gamma, has been reported to directly bind to eIF5 or eIF2B.
The evolution of the histone methyltransferase gene Su(var)3-9 in metazoans includes a fusion with and a re-fission from a functionally unrelated gene.
Sass et al., Leipzig, Germany. In Bmc Evol Biol, 2005
The loci of the major heterochromatic H3K9 methyltransferase Su(var)3-9 and the functionally unrelated gamma subunit of the translation initiation factor eIF2 are fused in Drosophila melanogaster.
Phylogenetic mapping of intron positions: a case study of translation initiation factor eIF2gamma.
Sass et al., Leipzig, Germany. In Mol Biol Evol, 2005
Eukaryotic translation initiation factor 2 (eIF2) is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon.
Cdc123 and checkpoint forkhead associated with RING proteins control the cell cycle by controlling eIF2gamma abundance.
Brenner et al., United States. In J Biol Chem, 2004
the Cdc123-Chf-Gcd11 axis is an essential pathway for nutritional control of START that runs parallel to the Tor-Gcn2-Sui2 system of translational control
Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B.
Wagner et al., Boston, United States. In Structure, 2004
The structural and functional similarities found between eIF2alpha/eIF2gamma and eEF1Balpha/eEF1A suggest a model for the interaction of eIF2alpha with eIF2gamma, and eIF2 with Met-tRNAiMet.
Substrates and signalling complexes: the tortured path to insulin action.
Kovacina et al., Stanford, United States. In J Cell Biochem, 1992
These putative substrates include: 1) pp15, a fatty acid-binding protein; 2) pp120, a plasma membrane ecto-ATPase; 3) pp42, a MAP serine/threonine kinase; 4) pp85, a subunit of the Type 1 phosphatidylinositol kinase; and 5) pp185, a phosphatidylinositol kinase binding protein.
Phosphorylation of c-jun mediated by MAP kinases.
Woodgett et al., London, United Kingdom. In Nature, 1991
We present evidence that mitogen-activated protein-serine (MAP) kinases (pp54 and pp42/44) specifically phosphorylate these sites and that their phosphorylation positively regulates the transacting activity of c-jun.
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